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At least 19 recordsLinked to original sources
PubMed1983

Transcriptional control of the fibronectin gene in chick embryo fibroblasts transformed by Rous sarcoma virus.

Rous sarcoma virus transformed-chick embryo fibroblasts contain decreased amounts of the adhesive protein fibronectin that results from a lowering of fibronectin mRNA levels (Fagan, J.B., Sobel, M.E., Yamada, K.M., de Crombrugghe, B., and Pastan, I. (1981) J. Biol. Chem. 256, 520-525). In the present study, nuclei isolated from chick embryo fibroblasts (CEF) and Rous sarcoma virus transformed-chick embryo fibroblasts (RSV-CEF) were used to measure relative rates of fibronectin RNA synthesis. [32P]RNA was synthesized by preinitiated endogenous RNA polymerases in nuclei, and the radioactive RNA was subsequently hybridized to DNA fragments spanning approximately 40 kilobase pairs (approximately 85%) of the fibronectin gene. Transformation of CEF by RSV resulted in a 7- to 8-fold reduction in the amount of 32P-labeled nuclear RNA hybridizing with fibronectin DNA sequences when the nuclei were incubated for either 3.5 or 45 min. These results indicate that decreased transcription and not reduced RNA stability plays a major role in lowering fibronectin mRNA levels in RSV-CEF. When nuclear RNA was transcribed in the presence of Sarkosyl, diminished RNA synthesis was still observed suggesting that reduced fibronectin transcription in RSV-CEF is not due to a block in RNA chain elongation. Our data indicate that transcriptional regulation of the fibronectin gene is an important mechanism of lowering steady state levels of fibronectin mRNA in RSV-CEF.

Animals↗
PubMed1973

Evidence for 30-40S RNA as precursor of the 60-70S RNA of Rous sarcoma virus.

Rous sarcoma virus harvested from cells at intervals of 3 min has the same density, sedimentation coefficient, and DNA polymerase as virus harvested at hourly intervals. The RNA of the Prague strain-C consists of a minor class of 60-70S RNA, a major class 30-40S RNA, and a 4-12S class of RNA present at variable concentration. The RNA of the Schmidt-Ruppin strain-A contains more 60-70S than 30-40S RNA. Upon incubation of virus harvested at 3-min intervals at 40 degrees in cell growth medium or Tris-saline, most of the 30-40S RNA is converted to 60-70S RNA. The electrophoretic mobility of the 30-40S RNA of the Rous virus harvested at 3-min intervals is lower than that of the 30-40S subunits of completely dissociated 60-70S RNA; after heating, their mobilities are identical. Heating also releases some small RNAs from 30-40S RNA of virus harvested at 3-min intervals, but five times more 4S RNA is released if the 30-40S RNA is allowed to convert to 60-70S in the virus. The template activity for Rous virus DNA polymerase of the 30-40S RNA of Rous virus harvested at 3-min intervals is about five times lower than that of 60-70S RNA. It is suggested that association of 30-40S RNAs with some RNAs of the 4-12S class may take place simultaneously with their conversion to 60-70S RNA.

Avian Sarcoma Viruses↗
PubMed1983

Transformation parameters and pp60src localization in cells infected with partial transformation mutants of Rous sarcoma virus.

Rous sarcoma virus (RSV)-induced transformation is mediated by the action of the viral src gene product pp60src. This transforming protein is found at several cytoplasmic locations, including the adhesion plaques of RSV-transformed cells. In these studies, we have focused on the adhesion plaque location of pp60src and determined whether any of the induced transformation parameters correlate with the presence of pp60src in the adhesion plaques. A series of partial transformation mutants of RSV that induce distinct transformation phenotypes were used, and infected chicken embryo cells were examined for (i) intracellular pp60src location, (ii) vinculin localization, (iii) abundance of phosphotyrosine on vinculin, (iv) integrity of stress fibers, and (v) expression of cell surface fibronectin. The results indicate that, among the limited number of mutants studied here, the presence of pp60src in adhesion plaques is independent of growth in soft agar and the increased phosphorylation of vinculin on tyrosine, but it does correlate with the loss of cell surface fibronectin. An elevated abundance of phosphotyrosine on vinculin is insufficient to cause stress fiber dissolution and is independent of the loss of fibronectin from the extracellular matrix. However, the increased relative amount of phosphotyrosine on vinculin is related to the ability of the cells to grow in soft agar. The adhesion plaque binding and tyrosine-specific kinase activities seem to represent two independent functions of pp60src.

Animals↗
PubMedDate not supplied

Studies on pp60src and associated kinase activity in regressing tumors induced by Rous sarcoma virus.

Rous sarcoma virus induced chicken tumors usually grow progressively for several weeks and then regress. pp60src kinase activity was reduced in cultured tumor cells which derived from regressing sarcomas by 60-75% as compared to progressively-growing neoplasms. We have demonstrated the presence of inhibitory activity to pp60src kinase activity in extracts of regressing tumor cells. Such extracts were able to reduced by 60% the level of kinase activity found in progressively-growing tumors, as measured in a IgG phosphorylation assay. Immunoprecipitation analyses of membrane or cytosol fractions did not reveal any significant differences between these two types of tumor cells in distribution of pp60src. The pp60src kinase of progressively-growing tumor cells was more sensitive than that of "regressor" cells to inhibition by P1, P4 di-(adenosine-5') tetraphosphate (Ap4 A) and to heat inactivation. These results suggest that the reduction of pp60src kinase activity in regressing neoplasms might be due to the presence of inhibitors in such cells, but that the basal levels of activity which remain are relatively resistant to further perturbation by heat and/or chemical antagonists.

Animals↗
PubMed1984

Homologies between a brain-specific identifier (ID) sequence and regions of Harvey murine sarcoma virus and Rous sarcoma virus genomes. Putative role of identifier sequences in the tissue specificity of malignant transformation by RNA tumor viruses.

As a step toward understanding of the tissue specificity of cellular transformation by RNA tumor viruses were looked for the presence of a putative brain specific regulatory (identifier) sequence (C82B) in the genome of various oncornaviruses. The genomes of Harvey murine sarcoma virus and Rous sarcoma virus contain sequences flanking the viral oncogenes with greater than 80% and greater than 60% homology to C82B, respectively. We suggest that identifier sequences acquired by oncoviruses may determine the potential target cells of malignant transformation after virus penetration.

Animals↗
PubMed1988

Suramin inhibits in vitro infection by duck hepatitis B virus, Rous sarcoma virus, and hepatitis delta virus.

Suramin blocked in vitro infection by duck hepatitis B virus, a hepadnavirus, and Rous sarcoma virus, a retrovirus. Although suramin was able to inhibit the virus-encoded reverse transcriptase activities of these two viruses, this inhibition did not appear to account for the anti-viral effect of the drug. In particular, suramin was unable to block synthesis within cells of full-length viral DNAs when added subsequent to infection. The results are consistent with the hypothesis that suramin acted by blocking virus uptake or uncoating. As further support of this hypothesis, we found that suramin also blocked infection by hepatitis delta virus, an RNA virus that is not known to employ reverse transcriptase during the initiation of infection.

Animals↗
PubMed1972

Rescue of rous sarcoma virus from rous sarcoma virus-transformed mammalian cells.

Rat cells transformed by the B77 strain of avian sarcoma virus produce no virus-like particles, yet B77 virus was rescued from these cells by Sendai virus-mediated fusion with chicken cells. This virus rescue was not affected by treatment of the chicken cells with agents that rendered the cells incapable of dividing, although such treatment greatly reduced the ability of the chicken cells to plate as infectious centers after infection with B77 virus. Fusion of R(B77) cells with chicken erythrocytes also led to virus rescue, although with less efficiency than fusion with chicken fibroblasts. Therefore, virus rescue was probably due to a factor or factors contributed by chicken cells which aid in virus production.

Animals↗
PubMed1982

Fusion injection of Rous Sarcoma virus proteins into Rous sarcoma virus-transformed, non-producing hamster cells causes release of infectious virus.

Purified virus proteins from transformation-defective (td) mutants of Rous sarcoma virus PrA or PrB were trapped in human erythrocyte ghosts which, after resealing, were fusion-injected into hamster RBH cells or rat TWERC cells. These cell lines are non-productively transformed by subgroup C Rous sarcoma virus. After fusion injection the hamster RBH cells released transforming subgroup C Rous sarcoma virus. No infectious virus could be rescued from rat TWERC cells. Since previous experiments have shown that fusion injection of the purified Rous sarcoma virus protein p15 into hamster RBH cells caused cleavage of the precursor protein pr76 to form the virus group-specific antigen (gag) but did not induce infectious virus, we conclude that in addition to p15 other virus proteins are required to induce virus rescue in hamster RBH cells.

Animals↗
PubMed1984

Cytoskeletal changes induced by two avian sarcoma viruses: UR2 and Rous sarcoma virus.

UR2-transformed cells were examined by immunofluorescence and compared to control cells and cells transformed by Rous Sarcoma Virus (RSV). Actin and tubulin which are normally depolymerized in RSV-transformed cells appeared to be unaffected by UR2 transformation. Cell surface fibronectin which is normally lost from RSV-infected cells, appears more abundantly on UR2-transformed cells than on normal cells. Vinculin was shown to be in adhesion plaques in UR2-transformed cells as well as in control fibroblasts but diffuse in the cytoplasm of RSV-transformed cells. Polyacrylamide gel electrophoresis of [35S]methionine-labeled fibronectin and vinculin immunoprecipitated from lysates of normal and transformed cells indicated that cell associated fibronectin synthesized during the labeling period is reduced by 60% in RSV-transformed cells but occurs in normal amounts in UR2-transformed cells. However, immunoprecipitation of radiolabeled fibronectin released in supernatant fluids of normal and transformed cells showed a decreased amount of fibronectin in fluids from UR2-transformed cells, but a considerable increase in the medium from RSV-infected cells as compared to uninfected cultures. These data suggest that more fibronectin binds to the surface of UR2-transformed cells then to normal cells, but is readily released from RSV-transformed cells. Vinculin was reduced by about 50% of normal levels in both RSV- and UR2-transformed cells. Immunofluorescence studies using antibody to virion structural proteins (gag) show that the nuclei of UR2-transformed cells are not fluorescent. This indicates a cytoplasmic location or membrane association for p68ros, the transforming protein of UR2, which contains gag determinants. Overall, these data suggest that changes in the major cytoskeletal proteins of fibroblasts are not essential for the neoplastic properties of cells but are rather a phenotypic expression of transformation, since UR2, which causes tumors in vivo, induces only minor cytoskeletal alterations of cells transformed in vitro.

Actins↗
PubMed1992

Partial characterization of rat cell lines infected by a Rous sarcoma virus-33.

Rous sarcoma virus-33 (RSV-33) was obtained from a sample of chicken Rous sarcoma which had been dried and stored in 1933. RSV-33, like the RSV-29, has the minimal number of passages beyond its isolation from chicken tumour No. 1. Our experiments demonstrated that the Rous sarcoma virus-33 was replication non-defective and was pathogenic for rats. Established rat tumorigenic cell lines express the viral genome. All three species of viral RNA were detected and v-src proteins and gag polyproteins were identified as well in cells of R9 and R74 lines. The virus can be rescued from cells of R9 and R74 lines, thus indicating that the cells are virogenic. The cells of a permanent tumorigenic line RT1 are infected but not transformed by RSV-33. Although they contain a complete proviral genome, they do not express detectable virus-specific RNA. The virus is not rescuable from RT1 cells under in vivo conditions. Proviral DNA analysis showed that the RSV-33 contained a full-length genome, including the env gene, in contrast to the RSV-29 which was found replication defective.

Animals↗
PubMed1972

Hybridization of Rous sarcoma virus deoxyribonucleic acid polymerase product and ribonucleic acids from chicken and rat cells infected with Rous sarcoma virus.

Rous sarcoma virus (RSV)-specific ribonucleic acid (RNA) in virus-producing chicken cells and non-virus-producing rat cells infected with RSV was studied by hybridization with the endogenous deoxyribonucleic acid (DNA) product of the RSV virion DNA polymerase system. By hybridizing the total DNA product with excess virion RNA, the product DNA was separated into hybridized ("minus") and nonhybridized ("plus") DNA. The "minus" DNA was complementary to at least 20% of the RNA from RSV which remained of high molecular weight after denaturation. A maximum of approximately 65% hybridization was observed between "minus" DNA and RSV RNA or RSV-infected chicken cell RNA. A maximum of about 60% hybridization was observed between "minus" DNA and RSV-infected rat cell RNA. RSV-infected chicken cells contained RSV-specific RNA equivalent to about 6,000 virions per cell. RSV-infected rat cells contained RSV-specific RNA equivalent to approximately 400 virions per cell. Neither cell type contained detectable RNA complementary to virion RNA. The RSV-specific RNA in RSV-infected rat cells did not appear to be qualitatively different from that in RSV-infected chicken cells.

Animals↗
PubMed1982

The increase in hormone-stimulated adenylate cyclase activity following Rous sarcoma virus transformation.

Rous sarcoma virus (RSV)-infected chicken embryo cells were used to study the effect of viral transformation on the hormone-stimulated synthesis of cyclic AMP. Transformation by RSV greatly increased the cells' ability to synthesize and accumulate cyclic AMP in response to the beta-adrenergic agonist isoproterenol as compared to untransformed cells. This enhancement was observed in both intact cells and in membranes prepared from these cells. The inclusion of guanosine 5'-0-(3-thiotriphosphate), a nonhydrolyzable analogue of GTP, in assays of adenylate cyclase activity did not abolish the quantitative differences between the transformed and normal cell membranes. Infection of cells by Rous-associated virus, which lacks the oncogene src, did not induce this hyperresponsiveness thus indicating the probable involvement of the src gene product in this phenomenon. The duration of the isoproterenol-induced cyclic AMP elevation was longer in the transformed than in the untransformed cells; transformed cells, unlike untransformed cells, required at least 120 min before full desensitization became established. Membranes prepared from transformed cells specifically bound more than 5 times the quantity of the beta-adrenergic radiolabeled antagonist (-)3H-dihydroalprenolol and 125I-iodocyanopindolol compared to the untransformed cell membranes. Thus, it appears that major differences between the transformed and normal phenotypes reside in the concentration of membrane beta-adrenergic receptors and the inability of RSV-transformed cells to self-limit their response to specific external stimuli.

Adenylyl Cyclases↗
PubMed1978

Simultaneous production of mouse endogenous virus and Rous sarcoma virus by Schmidt-Ruppin virus infected mouse cells.

Schmidt-Ruppin Rous sarcoma virus infected chick cells injected into newborn C3H/f mice gave rise to tumours at the site of inoculation. These tumours were transplantable in adult C3H/f mice and were able to induce tumours in the wing of adult Leghorn chickens. Tumour cells from the 18th passage in mice were used to establish a cell line in tissue culture (C3HSR). These cells released C-type virus particles that produced foci and were able to propagate in chick cells. Cloning of the C3HSR cells demonstrated that the same cell expressed both avian and murine antigens. Mouse cells infected with virus released by C3HSR cells produced murine leukaemia virus-like particles as revealed by the reverse XC syncytial test and by immunofluorescence tests.

Animals↗
PubMed1991

The isopycnic, compartmentalized integration of Rous sarcoma virus sequences.

Rous sarcoma virus (RSV) can cause tumors in hamsters, which harbor complete or partially deleted RSV sequences, in their genomes. Here we have studied the localization of RSV sequences integrated into the genome of cell lines derived from six independent hamster tumors. We have found that integration occurred in the isochores richest in guanine + cytosine, of the host genome, as it had been previously observed for bovine leukemia and hepatitis B viral sequences. The integration of RSV proviral sequences is, therefore, 'isopycnic' (i.e., it takes place in host genome sequences which compositionally match the viral sequences) and compartmentalized (i.e., it occurs in a small compositional compartment of the host genome). The hamster genome compartment hosting RSV sequences precisely corresponds to a compartment of the human genome which is the most active in both transcription and recombination. The notion of a compartmentalized, isopycnic integration of RSV proviral sequences fits, therefore, with the viral integration into transcriptionally active and recombinogenic regions of the host genome observed by other authors, but is broader, in that it includes, in addition, the requirement for a compositional match between host genome sequences and expressed viral sequences.

Animals↗
PubMed1980

Molecular events in cells transformed by Rous Sarcoma virus.

The Rous sarcoma virus (RSV) transforming gene product has been identified and characterized as a phosphoprotein with a molecular weight of 60,000, denoted pp60src. Partially purified pp60src displays a closely associated phosphotransferase activity with the unusual specificity of phosphorylating tyrosine residues in a variety of proteins. That the enzymatic activity observed is actually encoded by the RSV-transforming gene is indicated by the comparison of the pp60src-protein kinase isolated from cells tranformed by a wild-type RSV or by a RSV temperature-sensitive transformation mutant; these experiments revealed that the latter enzyme had a half-life of 3 min at 41 degrees C, whereas that of the wild-type enzyme was 20 min. Evidence is now beginning to accumulate showing that viral pp60src expresses its protein kinase activity in transformed cells as well as in vitro because at least one cellular protein has been identified as a substrate for this activity of pp60src. Although the protein kinase activity associated with pp60src is itself cyclic AMP (cAMP) independent, the molecule contains at least one serine residue that is directly phosphorylated by the cellular cAMP-dependent protein kinase, thus suggesting that the viral transforming gene product may be regulated indirectly by the level of cAMP. The significance of this latter observation must be regarded from the point of view that the RSV src gene is apparently derived from a normal cellular gene that seemingly expresses in normal uninfected cells a phosphoprotein structurally and functionally closely related to pp60src. This celluar protein, found in all vertebrate species tested, also is a substrate for a cAMP-dependent protein kinase of normal cells, and, therefore, may be evolved to function in a regulatory circuit involving cAMP.

Animals↗